MV3K_PICTO
ID MV3K_PICTO Reviewed; 324 AA.
AC Q6KZB1;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Mevalonate-3-kinase {ECO:0000303|PubMed:25636853};
DE Short=M3K {ECO:0000303|PubMed:25636853};
DE EC=2.7.1.185 {ECO:0000269|PubMed:25636853};
DE AltName: Full=ATP:(R)-mevalonate 3-phosphotransferase {ECO:0000250|UniProtKB:Q9HIN1};
DE Short=ATP:(R)-MVA 3 phosphotransferase {ECO:0000250|UniProtKB:Q9HIN1};
GN OrderedLocusNames=PTO1356 {ECO:0000312|EMBL:AAT43941.1};
OS Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC
OS 100828).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Picrophilaceae; Picrophilus.
OX NCBI_TaxID=263820;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828
RC {ECO:0000312|Proteomes:UP000000438};
RX PubMed=15184674; DOI=10.1073/pnas.0401356101;
RA Fuetterer O., Angelov A., Liesegang H., Gottschalk G., Schleper C.,
RA Schepers B., Dock C., Antranikian G., Liebl W.;
RT "Genome sequence of Picrophilus torridus and its implications for life
RT around pH 0.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9091-9096(2004).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE
RP SPECIFICITY, AND PATHWAY.
RX PubMed=25636853; DOI=10.1128/aem.04033-14;
RA Rossoni L., Hall S.J., Eastham G., Licence P., Stephens G.;
RT "The Putative mevalonate diphosphate decarboxylase from Picrophilus
RT torridus is in reality a mevalonate-3-kinase with high potential for
RT bioproduction of isobutene.";
RL Appl. Environ. Microbiol. 81:2625-2634(2015).
CC -!- FUNCTION: Catalyzes the phosphorylation of mevalonate (MVA) to yield
CC mevalonate-3-phosphate. Functions in an alternative mevalonate pathway,
CC which passes through mevalonate 3-phosphate rather than mevalonate 5-
CC phosphate. Also able to catalyze the formation of isobutene via the
CC conversion of 3-hydroxyisovalerate (3-HIV) to an unstable 3-phosphate
CC intermediate that undergoes a spontaneous decarboxylation.
CC {ECO:0000269|PubMed:25636853}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-mevalonate + ATP = (R)-3-phosphomevalonate + ADP + H(+);
CC Xref=Rhea:RHEA:42884, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:36464, ChEBI:CHEBI:82773, ChEBI:CHEBI:456216;
CC EC=2.7.1.185; Evidence={ECO:0000269|PubMed:25636853};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=23 uM for ATP {ECO:0000269|PubMed:25636853};
CC KM=131 uM for mevalonate {ECO:0000269|PubMed:25636853};
CC KM=2348 uM for 3-hydroxyisovalerate (3-HIV)
CC {ECO:0000269|PubMed:25636853};
CC KM=3163 uM for 3-hydroxybutyrate (3-HB)
CC {ECO:0000269|PubMed:25636853};
CC Note=kcat is 1.9 sec(-1) for mevalonate as substrate. kcat is 0.1
CC sec(-1) for 3-hydroxyisovalerate (3-HIV) as substrate. kcat is 0.1
CC sec(-1) for 3-hydroxybutyrate (3-HB) as substrate.
CC {ECO:0000269|PubMed:25636853};
CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis
CC via mevalonate pathway. {ECO:0000305|PubMed:25636853}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9HIN1}.
CC -!- SIMILARITY: Belongs to the GHMP kinase family. {ECO:0000305}.
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DR EMBL; AE017261; AAT43941.1; -; Genomic_DNA.
DR RefSeq; WP_011178157.1; NC_005877.1.
DR AlphaFoldDB; Q6KZB1; -.
DR SMR; Q6KZB1; -.
DR STRING; 263820.PTO1356; -.
DR EnsemblBacteria; AAT43941; AAT43941; PTO1356.
DR GeneID; 2845209; -.
DR KEGG; pto:PTO1356; -.
DR eggNOG; arCOG02937; Archaea.
DR HOGENOM; CLU_862228_0_0_2; -.
DR OMA; WNSYIVT; -.
DR OrthoDB; 77836at2157; -.
DR BRENDA; 2.7.1.185; 7518.
DR UniPathway; UPA00057; -.
DR Proteomes; UP000000438; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0019287; P:isopentenyl diphosphate biosynthetic process, mevalonate pathway; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.70.890; -; 1.
DR InterPro; IPR036554; GHMP_kinase_C_sf.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55060; SSF55060; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Isoprene biosynthesis; Kinase; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..324
FT /note="Mevalonate-3-kinase"
FT /id="PRO_0000439671"
FT BINDING 19
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9HIN1"
FT BINDING 109..112
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9HIN1"
FT BINDING 145
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9HIN1"
FT BINDING 149
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9HIN1"
FT BINDING 190
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9HIN1"
FT BINDING 193
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9HIN1"
SQ SEQUENCE 324 AA; 36791 MW; 8AFB60D0D781B40B CRC64;
MENYNVKTRA FPTIGIILLG GISDKKNRIP LHTTAGIAYT GINNDVYTET KLYVSKDEKC
YIDGKEIDLN SDRSPSKVID KFKHEILMRV NLDDENNLSI DSRNFNILSG SSDSGAAALG
ECIESIFEYN INIFTFENDL QRISESVGRS LYGGLTVNYA NGRESLTEPL LEPEAFNNFT
IIGAHFNIDR KPSNEIHENI IKHENYRERI KSAERKAKKL EELSRNANIK GIFELAESDT
VEYHKMLHDV GVDIINDRME NLIERVKEMK NNFWNSYIVT GGPNVFVITE KKDVDKAMEG
LNDLCDDIRL LKVAGKPQVI SKNF
